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Information on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase and Organism(s) Rattus norvegicus and UniProt Accession Q6AYS7

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EC Tree
IUBMB Comments
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q6AYS7
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aminoacylase, acylase i, acy-1, aminoacylase i, aminoacylase 1, aminoacylase-1, l-aminoacylase, l-acy-1, aaiii, pacy1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacylase 1
-
aminoacylase 1a
-
aminoacylase-1A
-
N-acyl-L-amino-acid amidohydrolase
-
acylase
-
-
-
-
acylase I
-
-
-
-
alpha-N-acylaminoacid hydrolase
-
-
-
-
amido acid deacylase
-
-
-
-
aminoacylase I
-
-
-
-
benzamidase
-
-
-
-
dehydropeptidase II
-
-
-
-
hippurase
-
-
-
-
hippuricase
-
-
-
-
histozyme
-
-
-
-
L-amido-acid acylase
-
-
-
-
L-aminoacylase
-
-
-
-
long acyl amidoacylase
-
-
-
-
N-acyl-L-amino-acid amidohydrolase
-
-
-
-
N-acylase IA
-
-
N-formylmethionine deformylase
-
-
Nalpha-acyl-L-amino acid amidohydrolase
-
-
short acyl amidoacylase
-
-
-
-
additional information
the enzyme is a member of the metalloprotein family M20
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
show the reaction diagram
active site structure, molecular modelling to determine Asp82 function in catalysis, Asp82 ensures a proper protonation of the catalytic His residue, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deacylation
-
-
-
-
hydrolysis of amide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-alpha-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-37-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-leucine + H2O
acetate + L-leucine
show the reaction diagram
-
-
-
?
N-acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
?
acetyl-L-methionine + H2O
acetate + L-methionine
show the reaction diagram
-
-
-
-
?
N-acetyl-DL-methionine + H2O
DL-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-2-aminopentanoate + H2O
acetate + L-2-aminopentanoate
show the reaction diagram
-
-
-
-
?
N-acetyl-L-cysteine + H2O
acetate + L-cysteine
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
N-acetylmethionine + H2O
acetate + L-methionine
show the reaction diagram
-
preferred substrate
-
-
?
N-acetylseleno-L-methionine + H2O
acetate + L-selenomethionine
show the reaction diagram
-
-
-
-
?
N-formylmethionine + H2O
formate + L-methionine
show the reaction diagram
-
substrate synthesis and purification, overview
-
-
?
O-methyl-N-acetyl-DL-serine + H2O
acetate + O-methyl-DL-serine
show the reaction diagram
-
-
-
-
?
S-(1,1,2,2-tetrafluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(-1,1,2,2-terafluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-(2-bromo-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(2-bromo-1,1,2-trifluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-(2-chloro-1,1,2-trifluoroethyl)-N-acetyl-L-cysteine + H2O
acetate + S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine
show the reaction diagram
-
-
-
-
?
S-ethyl-N-acetyl-L-cysteine + H2O
acetate + S-ethyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-isobutyl-N-acetyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-isopropyl-N-acetyl-L-cysteine + H2O
acetate + S-isopropyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-methyl-N-acetyl-L-cysteine + H2O
acetate + S-methyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-n-butyl-N-acetyl-L-cysteine + H2O
acetate + S-n-butyl-L-cysteine
show the reaction diagram
-
-
-
-
?
S-n-propyl-N-acetyl-L-cysteine + H2O
acetate + S-n-propyl-L-cysteine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-methionine
L-methionine + acetate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in the degradation of chemotactic N-formyl peptides and plays a protective role in degrading bacterial and mitochondrial N-formylated peptide together with the alpha-N-acylpeptide hydrolase, EC 3.4.19.1
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
metalloenzyme, required for activity
CoCl2
-
activates 2-3fold at 0.1 mM
NiCl2
-
activates 2-3fold at 0.1 mM
Zn2+
-
0.98 Zn2+ per enzyme molecule, tightly bound, involved in cataylsis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
6% inhibition at 10 mM
DTT
-
85% inhibition at 20 mM
EDTA
-
10% inhibition at 50 mM
iodoacetamide
-
90% inhibition at 10 mM
N-acetyl-L-2-aminohexanoic acid
-
-
n-butylmalonic acid
-
-
Nepsilon-formyl-Nepsilon-hydroxy-L-lysine
-
IC50: 1.0 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4
N-acetyl-L-cysteine
-
-
2.1
N-acetyl-L-methionine
-
-
0.3
N-acetylmethionine
-
pH 8.0, 22°C
4
N-acetylseleno-L-methionine
-
-
3.1
N-formylmethionine
-
pH 8.0, 22°C
3.4
S-ethyl-N-acetyl-L-cysteine
-
-
2.1
S-methyl-N-acetyl-L-cysteine
-
-
3.7
S-n-butyl-N-acetyl-L-cysteine
-
-
0.8
S-n-propyl-N-acetyl-L-cysteine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
N-acetylmethionine
-
pH 8.0, 22°C
7.9
N-formylmethionine
-
pH 8.0, 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
Nepsilon-formyl-Nepsilon-hydroxy-L-lysine
Rattus norvegicus
-
IC50: 1.0 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.2
-
purified enzyme
8.33
-
pH 8.0, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACY1A_RAT
408
0
45804
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
x * 45000, SDS-PAGE
125000
-
gel filtration
43000
-
2 * 43000, SDS-PAGE
44000
-
gel filtration
45000
-
gel filtration
45847
-
3 * 45847, deduced from deduced aminacid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
monomer
trimer
additional information
structure molecular modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C23A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C272A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C294A
site-directed mutagenesis, the mutation causes a conformational change of the 3D-structure, the mutant shows highly reduced activity compared to the wild-type enzyme
C331A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
C49A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
D82E
site-directed mutagenesis, the mutant shows highly reduced activity and loss of zinc coordination compared to the wild-type enzyme
D82N
site-directed mutagenesis, nearly inactive mutant
E147A
-
completely inactive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from bacteria by solubilization with Triton X-100 and 10% sarcosyl, glutathione affinity chromatography, and tag removal by thrombin
by a method that includes DEAE-Sepharose column, Chelating-Sepharose column, Amicon PM 30 membrane and Sephacryl-S200 column
-
native enzyme from intestinal epithelial mucosa, 1833fold to homogeneity, by acid precipitation, two steps of anion exchange chromatography, hydrophobic interaction chromatography, gel filtration and concanavalin A afinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACYI, DNA and amino acid sequence determination and analysis, comparison with the porcine intestinal enzyme
expression of GST-tagged wild-type and mutant enzymes in bacteria
expressed in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
N-acetyl-L-cysteine used for drugs against lung disorders and HIV infections, test of potential antitumor agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uttamsingh, V.; Keller, D.A.; Anders, M.W.
Acylase I-catalyzed deacetylatin of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines
Chem. Res. Toxicol.
11
801-809
1998
Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Durand, A.; Giardina, T.; Villard, C.; Roussel, A.; Puigserver, A.; Perrier, J.
Rat kidney acylase I: further characterization and mutation studies on the involvement of Glu 147 in the catalytic process
Biochimie
85
953-962
2003
Rattus norvegicus
Manually annotated by BRENDA team
Herga, S.; Brutus, A.; Vitale, R.M.; Miche, H.; Perrier, J.; Puigserver, A.; Scaloni, A.; Giardina, T.
Site-directed mutagenesis and molecular modelling studies show the role of Asp82 and cysteines in rat acylase 1, a member of the M20 family
Biochem. Biophys. Res. Commun.
330
540-546
2005
Rattus norvegicus (Q6AYS7)
Manually annotated by BRENDA team
Nguyen, K.T.; Pei, D.
Purification and characterization of enzymes involved in the degradation of chemotactic N-formyl peptides
Biochemistry
44
8514-8522
2005
Rattus norvegicus
Manually annotated by BRENDA team
Perrier, J.; Durand, A.; Giardina, T.; Puigserver, A.
The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme
Comp. Biochem. Physiol. B
138B
277-283
2004
Sus scrofa (P37111), Rattus norvegicus (Q6AYS7)
-
Manually annotated by BRENDA team
Zhong, Y.; Onuki, J.; Yamasaki, T.; Ogawa, O.; Akatsuka, S.; Toyokuni, S.
Genome-wide analysis identifies a tumor suppressor role for aminoacylase 1 in iron-induced rat renal cell carcinoma
Carcinogenesis
30
158-164
2009
Rattus norvegicus (Q6AYS7)
Manually annotated by BRENDA team